Immunodeficiency virus protease

From Proteopedia

Template:STRUCTURE 1hhp HIV is a notoriously lethal virus that is known to cause AIDS. There currently is no cure or vaccine. But, scientists have discovered treatments that can slow progression of the HIV virus, thanks in large part to our understanding of the structure of HIV-1 protease, seen here on the right in complex with a potent drug used for slowing the progression of HIV, .

HIV-1 protease is a protein made by the HIV virus that is crucial to the virus's infectious capacity. The virus makes certain proteins that need to be cleaved, or cut, in order to transform into mature, fully-functional proteins that can allow the virus to infect new cells. HIV-1 protease is responsible for cleaving these nascent proteins into their mature form.

Saquinavir was the the first FDA approved protease inhibitor.

Looking at the structure of HIV-1 protease, we see that the protein is composed of . Each subunit consists of the same small chain of only 99 amino acids. The subunits come together in such as way as to . The protein to-be-cleaved sits in this tunnel. In the middle of the tunnel is the active site of the protease: an Asp-Thr-Gly (25, 26, and 27) catalytic triad withthe two Asps acting as the catalytic residues.

(large scene, takes a while to load) to allow proteins to enter the tunnel.

PAGE IN PROGRESS Eran Hodis 19:10, 15 August 2008 (IDT)

This page is not a fully developed page, but was created as an example for the press release of the Proteopedia article in the open-access journal Genome Biology. Please expand this page with additional information and references.